Ubiquitin-agarose is used in affinity chromatography, protein chromatography, intracellular protein degradation, calpain and lysosomal proteases, proteomics, specialty resins and ubiquitination analysis. Ubiquitin-agarose has been used in a study to produce evidence for a particulate location of ubiquitin conjugates and ubiquitin-conjugating enzymes in the rabbit brain. Ubiquitin-agarose has also been used to study fertilization of the ascidian, Halocynthia roretzi.
Physical form
Suspension in 1 M NaCl containing 15 Mm Sodium azide.
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Retroviral Gag polyprotein precursors are both necessary and sufficient for the assembly and release of virus-like particles (VLPs) from infected cells. It is well established that small Gag-encoded motifs, known as late domains, promote particle release by interacting with components
The Journal of pathology, 203(1), 603-608 (2004-04-20)
Although the key event in the pathology of prion diseases is thought to be the conversion of cellular prion protein (PrP(C)) to the protease-resistant scrapie species termed PrP(Sc), the factors that contribute to neurodegeneration in scrapie-infected animals are poorly understood.
European journal of biochemistry, 255(2), 482-491 (1998-08-26)
Ubiquitin is often implicated as a specific tag for protein degradation via the ubiquitin system although only a limited number of physiological proteins have been shown to be degraded in their native tissues via this pathway in vivo. Ubiquitin may
The Journal of biological chemistry, 257(5), 2537-2542 (1982-03-10)
We have previously described an enzyme that activates ubiquitin, the heat-stable polypeptide of the ATP-dependent proteolytic system from reticulocytes (Ciechanover, A., Heller, H., Katz-Etzion, R., and Hershko, A. (1981) Proc. Natl. Acad. Sci. U. S. A. 78, 761-765). It carries
The Journal of biological chemistry, 280(20), 19600-19606 (2005-03-10)
Ubiquitination serves as a key sorting signal in the lysosomal degradation of endocytosed receptors through the ability of ubiquitinated membrane proteins to be recognized and sorted by ubiquitin-binding proteins along the endocytic route. The ESCRT-II complex in yeast contains one
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